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Last Updated: 3 years ago

Possible Interaction: Caseins and Trypsin

supplement:

Caseins

supplement:

Trypsin

Research Papers that Mention the Interaction

Trypsin that can hydrolyze CS during dissolution resulted in further enhancement of MA dissolution from the physical and kneaded mixtures.
AAPS PharmSciTech  •  2016  |  View Paper
Even the completely digested products of casein with trypsin or chymotrypsin showed inhibitory activities against the two proteases.
It was suggested that not only the intact casein but also the products digested with trypsin or chymotrypsin contribute to the inhibitory effect of casein on the proteases in the intestinal lumen.
Pharmaceutical Research  •  2004  |  View Paper
Casein strongly inhibited trypsin and chymotrypsin in the concentration-dependent manner.
Casein was shown to have strong inhibitory activity on trypsin and chymotrypsin in the intestinal lumen.
Pharmaceutical Research  •  2004  |  View Paper
Decreased inhibitory activity of the trypsin domain was observed with casein and benzoyl arginine ethyl ester as substrates.
Biochimica et biophysica acta  •  1993  |  View Paper
Intraduodenal administration of casein in a dose of 400 mg/h caused significant increases in plasma CCK concentration and pancreatic secretion of juice volume and outputs of amylase and trypsin.
Pancreas  •  1989  |  View Paper
Furthermore, the plasma CCK response to casein was completely abolished by the simultaneous administration of trypsin.
The American journal of physiology  •  1986  |  View Paper
Trypsinization decreased the Km of phosphatase for casein from 10.8 to 1.2 microM and increased the Vmax from 4.9 to 30.9 nmol (mg of protein)-1 min-1.
Biochemistry  •  1984  |  View Paper
It was found that conjugated trypsin required lower incubation periods for complete hydrolysis of casein , BSA & ovalbumin as compared to free enzyme.
Colloids and surfaces. B, Biointerfaces  •  2019  |  View Paper
The relative activity of immobilized TRY in the hydrolysis of casein was higher than that of the free enzyme over broader temperature ranges.
Journal of colloid and interface science  •  2012  |  View Paper
Zymography analysis showed that both trypsins were active in degrading casein.
Food chemistry  •  2008  |  View Paper
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